The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Structural studies on human 2-oxoglutarate dependent oxygenases
Abstract
2-Oxoglutarate and ferrous iron-dependent oxygenases have emerged as an important family of human enzymes that catalyse hydroxylations and related demethylation reactions. Their substrates in humans include proteins, nucleic acids, lipids and small molecules. They play roles in collagen biosynthesis, hypoxic sensing, regulation of gene expression and lipid biosynthesis/metabolism. Structural analyses, principally employing crystallography, have revealed that all of these oxygenases possess a double-stranded β-helix core fold that supports a highly conserved triad of iron binding residues and a less well conserved 2-oxoglutarate co-substrate binding site. The 2-oxoglutarate binds to the iron in a bidentate manner via its 1-carboxylate and 2-oxo groups. The primary substrate binding elements are more variable and can involve mobile elements.
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“The largest group of enzymes using vitamin C as one of their cofactors is the iron-dependent and 2-oxoglutarate-dependent dioxygenases superfamily (2OGO, α-ketoglutarate-dependent hydroxylases). In humans, it represents about 80 enzymes responsible for the modification of important biological substances and processes (Table 2) [97,98,99].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [97]
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The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate-Dependent Nucleic Acid Demethylase
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Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937
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Research works printed but not linked: 1
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Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553
2-Oxoglutarate-Dependent Oxygenases
Islam, M. S., Leissing, T. M., Chowdhury, R., Hopkinson, R. J., & Schofield, C. J. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044724 · Cited by 472
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Metadata
- Authors
- McDonough, M. A., Loenarz, C., Chowdhury, R., Clifton, I. J., & Schofield, C. J.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Schofield, Christopher J
- ORCID
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 20
- Issue
- 6
- Pages
- 659-672
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2069351864
- Cited by
- 280
- References
- 73
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 16 · 2023: 15 · 2022: 20 · 2021: 13 · 2020: 27 · 2019: 16 · 2018: 18 · 2017: 15 · 2016: 20 · 2015: 29 · 2014: 33 · 2013: 16 · 2012: 16
- FWCI
- 0.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- European Commission
- Biotechnology and Biological Sciences Research Council (BB/D011523/1, BB/F006349/1)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- 2-oxoglutarate-dependent dioxygenase, substrate binding, collagen synthesis, gene expression regulation, lipid metabolism, crystal structure
- MeSH terms
- Animals, Fatty Acids, Humans, Hydroxylation, Ketoglutaric Acids, Nucleic Acids, Oxygenases, Biocatalysis
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